Unfolding and extraction of a transmembrane alpha-helical peptide: dynamic force spectroscopy and molecular dynamics simulations.

Journal article

An atomic force microscope (AFM) was used to visualize CWALP(19)23 peptides ((+)H(3)N-ACAGAWWLALALALALALALWWA-COO(-)) inserted in gel-phase DPPC and DSPC bilayers. The peptides assemble in stable linear structures and domains. A model for the organization of the peptides is given from AFM images and a 20 ns molecular dynamics (MD) simulation. Gold-coated AFM cantilevers were used to extract single peptides from the bilayer through covalent bonding to the cystein residue. Experimental and simu...

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Authors: Contera, SA; Lemaître, V; de Planque, MR; Watts, A; Ryan, J

• Publication status: Published
• Journal: Biophysical journal
• Volume: 89
• Issue: 5
• Pages: 3129-3140
• Publication date: 2005-11-01
• DOI: 10.1529/biophysj.105.061721
• EISSN: 1542-0086
• ISSN: 0006-3495
• Language: English
• Keywords: Carnitine; Lipid Bilayers; Cell Adhesion; Cell Membrane; Peptides; Protein Structure, Secondary; 1,2-Dipalmitoylphosphatidylcholine; Hot Temperature; Molecular Conformation; Spectrum Analysis; Spectrophotometry; Protein Folding; Pyrenes; Tryptophan; Protein Denaturation; Microscopy, Atomic Force; Phosphatidylcholines; Thermodynamics; Computer Simulation; Models, Molecular